scholarly journals Atg11 Links Cargo to the Vesicle-forming Machinery in the Cytoplasm to Vacuole Targeting Pathway

2005 ◽  
Vol 16 (4) ◽  
pp. 1593-1605 ◽  
Author(s):  
Tomohiro Yorimitsu ◽  
Daniel J. Klionsky
Keyword(s):  
Self Assembly ◽  
Coiled Coil ◽  
Vesicle Formation ◽  
Selective Autophagy ◽  
C Terminus ◽  
Central Regions ◽  
Putative Site ◽  
Integral Role ◽  
Cargo Molecule

Proteins are selectively packaged into vesicles at specific sites and then delivered correctly to the various organelles where they function, which is critical to the proper physiology of each organelle. The precursor form of the vacuolar hydrolase aminopeptidase I is a selective cargo molecule of the cytoplasm to vacuole targeting (Cvt) pathway and autophagy. Precursor Ape1 along with its receptor Atg19 forms the Cvt complex, which is transported to the pre-autophagosomal structure (PAS), the putative site of Cvt vesicle formation, in a process dependent on Atg11. Here, we show that this interaction occurs through the Atg11 C terminus; subsequent recruitment of the Cvt complex to the PAS depends on central regions within Atg11. Atg11 was shown to physically link several proteins, although the timing of these interactions and their importance are unknown. Our mapping shows that the Atg11 coiled-coil domains are involved in self-assembly and the interaction with other proteins, including two previously unidentified partners, Atg17 and Atg20. Atg11 mutants defective in the transport of the Cvt complex to the PAS affect the localization of other Atg components, supporting the idea that the cargo facilitates the organization of the PAS in selective autophagy. These findings suggest that Atg11 plays an integral role in connecting cargo molecules with components of the vesicle-forming machinery.

scholarly journals Segregation and activation of myosin IIB creates a rear in migrating cells

2008 ◽  
Vol 183 (3) ◽  
pp. 543-554 ◽  
Author(s):  
Miguel Vicente-Manzanares ◽  
Margaret A. Koach ◽  
Leanna Whitmore ◽  
Marcelo L. Lamers ◽  
Alan F. Horwitz
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Coiled Coil ◽  
Myosin Isoforms ◽  
C Terminus ◽  
Filament Bundles ◽  
A Cell ◽  
Myosin Iia ◽  
And Function ◽  
Migrating Cells

We have found that MLC-dependent activation of myosin IIB in migrating cells is required to form an extended rear, which coincides with increased directional migration. Activated myosin IIB localizes prominently at the cell rear and produces large, stable actin filament bundles and adhesions, which locally inhibit protrusion and define the morphology of the tail. Myosin IIA forms de novo filaments away from the myosin IIB–enriched center and back to form regions that support protrusion. The positioning and dynamics of myosin IIA and IIB depend on the self-assembly regions in their coiled-coil C terminus. COS7 and B16 melanoma cells lack myosin IIA and IIB, respectively; and show isoform-specific front-back polarity in migrating cells. These studies demonstrate the role of MLC activation and myosin isoforms in creating a cell rear, the segregation of isoforms during filament assembly and their differential effects on adhesion and protrusion, and a key role for the noncontractile region of the isoforms in determining their localization and function.

The SPI2-encoded SseA chaperone has discrete domains required for SseB stabilization and export, and binds within the C-terminus of SseB and SseD

Microbiology ◽  
2004 ◽  
Vol 150 (7) ◽  
pp. 2055-2068 ◽  
Author(s):  
Daniel V. Zurawski ◽  
Murry A. Stein
Keyword(s):  
Type Iii Secretion ◽  
Coiled Coil ◽  
Amphipathic Helix ◽  
Yeast Two Hybrid ◽  
C Terminus ◽  
N Terminus ◽  
Domain Mapping ◽  
Self Association ◽  
Discrete Domains ◽  
Two Hybrid

SseA, a key Salmonella virulence determinant, is a small, basic pI protein encoded within the Salmonella pathogenicity island 2 and serves as a type III secretion system chaperone for SseB and SseD. Both SseA partners are subunits of the surface-localized translocon module that delivers effectors into the host cell; SseB is predicted to compose the translocon sheath and SseD is a putative translocon pore subunit. In this study, SseA molecular interactions with its partners were characterized further. Yeast two-hybrid screens indicate that SseA binding requires a C-terminal domain within both partners. An additional central domain within SseD was found to influence binding. The SseA-binding region within SseB was found to encompass a predicted amphipathic helix of a type participating in coiled-coil interactions that are implicated in the assembly of translocon sheaths. Deletions that impinge upon this putative coiled-coiled domain prevent SseA binding, suggesting that SseA occupies a portion of the coiled-coil. SseA occupancy of this motif is envisioned to be sufficient to prevent premature SseB self-association inside bacteria. Domain mapping on the chaperone was also performed. A deletion of the SseA N-terminus, or site-directed mutations within this region, allowed stabilization of SseB, but its export was disrupted. Therefore, the N-terminus of SseA provides a function that is essential for SseB export, but dispensable for partner binding and stabilization.

scholarly journals Reggie/flotillin proteins are organized into stable tetramers in membrane microdomains

2007 ◽  
Vol 403 (2) ◽  
pp. 313-322 ◽  
Author(s):  
Gonzalo P. Solis ◽  
Maja Hoegg ◽  
Christina Munderloh ◽  
Yvonne Schrock ◽  
Edward Malaga-Trillo ◽  
...  
Keyword(s):  
T Cell Activation ◽  
Cell Activation ◽  
Coiled Coil ◽  
Cellular Prion Protein ◽  
Membrane Microdomains ◽  
Protein Assemblies ◽  
Cellular Processes ◽  
C Terminus ◽  
Functional Relevance ◽  
Interfering Rna

Reggie-1 and -2 proteins (flotillin-2 and -1 respectively) form their own type of non-caveolar membrane microdomains, which are involved in important cellular processes such as T-cell activation, phagocytosis and signalling mediated by the cellular prion protein and insulin; this is consistent with the notion that reggie microdomains promote protein assemblies and signalling. While it is generally known that membrane microdomains contain large multiprotein assemblies, the exact organization of reggie microdomains remains elusive. Using chemical cross-linking approaches, we have demonstrated that reggie complexes are composed of homo- and hetero-tetramers of reggie-1 and -2. Moreover, native reggie oligomers are indeed quite stable, since non-cross-linked tetramers are resistant to 8 M urea treatment. We also show that oligomerization requires the C-terminal but not the N-terminal halves of reggie-1 and -2. Using deletion constructs, we analysed the functional relevance of the three predicted coiled-coil stretches present in the C-terminus of reggie-1. We confirmed experimentally that reggie-1 tetramerization is dependent on the presence of coiled-coil 2 and, partially, of coiled-coil 1. Furthermore, since depletion of reggie-1 by siRNA (small interfering RNA) silencing induces proteasomal degradation of reggie-2, we conclude that the protein stability of reggie-2 depends on the presence of reggie-1. Our data indicate that the basic structural units of reggie microdomains are reggie homo- and hetero-tetramers, which are dependent on the presence of reggie-1.

Self-assembly of Stimuli Responsive Coiled-coil Fibrous Hydrogels

Soft Matter ◽  
2021 ◽  
Author(s):  
Michael Meleties ◽  
Priya Katyal ◽  
Bonnie Lin ◽  
Dustin Britton ◽  
Jin Kim Montclare
Keyword(s):  
Drug Delivery ◽  
Tissue Engineering ◽  
Self Assembly ◽  
Coiled Coil ◽  
Stimuli Responsive ◽  
Tunable Properties ◽  
Stimuli Sensitive ◽  
Biomedical Fields

Owing to their tunable properties, hydrogels comprised of stimuli sensitive polymers are one of the most appealing scaffolds with applications in tissue engineering, drug delivery and other biomedical fields. We...

scholarly journals The kfrA gene is the first in a tricistronic operon required for survival of IncP-1 plasmid R751

Microbiology ◽  
2006 ◽  
Vol 152 (6) ◽  
pp. 1621-1637 ◽  
Author(s):  
Malgorzata Adamczyk ◽  
Patrycja Dolowy ◽  
Michal Jonczyk ◽  
Christopher M. Thomas ◽  
Grazyna Jagura-Burdzy
Keyword(s):  
Coiled Coil ◽  
Broad Host Range ◽  
Gram Negative Bacteria ◽  
Bacterial Cells ◽  
Wild Type ◽  
C Terminus ◽  
Low Copy Number ◽  
And Control ◽  
Broad Host Range Plasmids

The kfrA gene of the IncP-1 broad-host-range plasmids is the best-studied member of a growing gene family that shows strong linkage to the minimal replicon of many low-copy-number plasmids. KfrA is a DNA binding protein with a long, alpha-helical, coiled-coil tail. Studying IncP-1β plasmid R751, evidence is presented that kfrA and its downstream genes upf54.8 and upf54.4 were organized in a tricistronic operon (renamed here kfrA kfrB kfrC), expressed from autoregulated kfrAp, that was also repressed by KorA and KorB. KfrA, KfrB and KfrC interacted and may have formed a multi-protein complex. Inactivation of either kfrA or kfrB in R751 resulted in long-term accumulation of plasmid-negative bacteria, whereas wild-type R751 itself persisted without selection. Immunofluorescence studies showed that KfrAR751 formed plasmid-associated foci, and deletion of the C terminus of KfrA caused plasmid R751ΔC 2 kfrA foci to disperse and mislocalize. Thus, the KfrABC complex may be an important component in the organization and control of the plasmid clusters that seem to form the segregating unit in bacterial cells. The studied operon is therefore part of the set of functions needed for R751 to function as an efficient vehicle for maintenance and spread of genes in Gram-negative bacteria.

scholarly journals Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52

2021 ◽  
Vol 7 (33) ◽  
pp. eabi6582
Author(s):  
Tao Fu ◽  
Mingfang Zhang ◽  
Zixuan Zhou ◽  
Ping Wu ◽  
Chao Peng ◽  
...  
Keyword(s):  
Protein Complex ◽  
Coiled Coil ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid ◽  
Related Protein ◽  
Binding Region ◽  
Receptor Associated Protein ◽  
Selective Autophagy ◽  
Specific Association ◽  
Molecular Bases

The recruitment of Unc-51-like kinase and TANK-binding kinase 1 complexes is essential for Nuclear dot protein 52-mediated selective autophagy and relies on the specific association of NDP52, RB1-inducible coiled-coil protein 1, and Nak-associated protein 1 (5-azacytidine-induced protein 2, AZI2). However, the underlying molecular mechanism remains elusive. Here, we find that except for the NDP52 SKIP carboxyl homology (SKICH)/RB1CC1 coiled-coil interaction, the LC3-interacting region of NDP52 can directly interact with the RB1CC1 Claw domain, as that of NAP1 FIP200-binding region (FIR). The determined crystal structures of NDP52 SKICH/RB1CC1 complex, NAP1 FIR/RB1CC1 complex, and the related NAP1 FIR/Gamma-aminobutyric acid receptor-associated protein complex not only elucidate the molecular bases underpinning the interactions of RB1CC1 with NDP52 and NAP1 but also reveal that RB1CC1 Claw and Autophagy-related protein 8 family proteins are competitive in binding to NAP1 and NDP52. Overall, our findings provide mechanistic insights into the interactions of NDP52, NAP1 with RB1CC1 and ATG8 family proteins.

Selective Vesicle Formation from Calixarenes by Self-Assembly

1999 ◽  
Vol 38 (4) ◽  
pp. 504-506 ◽  
Author(s):  
Yasutaka Tanaka ◽  
Masami Miyachi ◽  
Yoshiaki Kobuke
Keyword(s):  
Self Assembly ◽  
Vesicle Formation

Size-Defined Cracked Vesicle Formation via Self-Assembly of Gold Nanoparticles Covered with Carboxylic Acid-Terminated Surface Ligands

Langmuir ◽  
2018 ◽  
Vol 34 (41) ◽  
pp. 12445-12451 ◽  
Author(s):  
Jinjian Wei ◽  
Hideyuki Mitomo ◽  
Takeharu Tani ◽  
Yasutaka Matsuo ◽  
Kenichi Niikura ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Carboxylic Acid ◽  
Self Assembly ◽  
Vesicle Formation ◽  
Surface Ligands

scholarly journals Colloidal stability versus self-assembly of nanoparticles controlled by coiled-coil protein interactions

Soft Matter ◽  
2019 ◽  
Vol 15 (36) ◽  
pp. 7122-7126
Author(s):  
Allison Siehr ◽  
Bin Xu ◽  
Ronald A. Siegel ◽  
Wei Shen
Keyword(s):  
Protein Interactions ◽  
Self Assembly ◽  
Colloidal Stability ◽  
Coiled Coil ◽  
Biomolecular Recognition

Orientational discrimination of biomolecular recognition is exploited to control nanoparticle self assembly and colloidal stability.

scholarly journals Rational Design of Helical Nanotubes from Self-assembly of Coiled-coil Lock Washers

2013 ◽  
Vol 19 (S2) ◽  
pp. 342-343
Author(s):  
C. Xu ◽  
E.R. Wright ◽  
A. Mehta ◽  
L.C. Ser-pell ◽  
X. Zuo ◽  
...  
Keyword(s):  
Self Assembly ◽  
Rational Design ◽  
Coiled Coil

Extended abstract of a paper presented at Microscopy and Microanalysis 2013 in Indianapolis, Indiana, USA, August 4 – August 8, 2013.

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